Tyrosinase (T3824)

Home , Oxidase, Oxidoreductase, Tyrosinase

Catalog Number T3824 Storage Temperature –20 C

CAS RN 9002-10-2 Unit Definition: One unit will cause an increase in A280 EC 1.14.18.1 of 0.001 per minute at pH 6.5 at 25 C, in a 3 ml Synonyms: Monophenol monooxygenase; reaction mix containing L-tyrosine. Monophenol, dihydroxyphenylalanine:oxygen oxidoreductase Precautions and Disclaimer This product is for R&D use only, not for drug, Product Description household, or other uses. Please consult the Safety Tyrosinase is a copper-containing oxidase which has Data Sheet for information regarding hazards and safe activity on both catechols and cresol. It is responsible handling practices. for browning reactions. Tyrosinase is reported to have two binding sites for aromatic substrates and a different Preparation Instructions binding site for oxygen, the copper-containing site.1 Tyrosinase is soluble (2 mg/ml) in 50 mM potassium phosphate buffer, pH 6.5, yielding a clear brown Overall Reaction: solution.

O O O O Storage/Stability H2N CH O OH H2N CH O OH H2N CH O OH H N CH O OH 2 When stored at –20 C, the product loses 5% activity CH2 CH2 CH2 CH2 Tyrosinase per year. If stored at 37 C, 40–60% activity is lost in O2 H2O 7 days.7 OH OH O OH OH OH O Solutions retain activity for several days at 4–8 C and L-Tyrosine L-DOPA L-DOPA L-DOPA Quinone for several weeks frozen at –20 C.6 The enzyme is 4 2 rapidly denatured in 1% SDS solution. It dissociates KM for L-Tyrosine: 0.5 mM K for L-DOPA:2 1.5 mM into subunits in saturated urea and is completely M inactivated. While the dissociation is reversible, the 6 Catechol acts as a suicide substrate for tyrosinase, inactivation is not. causing irreversible inactivation during catechol oxidation.3 Tyrosinase is also inhibited by compounds References that complex with copper, such as benzoic acid and 1. Duckworth, H.W., and Colman, J.E., J. Biol. Chem., cyanide. Benzoic acid inhibition is competitive with 245(7), 1613-1625 (1970). catechol. Cyanide inhibition is competitive with oxygen 2. Espin, J.C. et al., J. Agric. Food Chem., 47(9), and noncompetitive with catechol.1 3495-3502 (1999). 3. Cánovas, F.G. et al., Biochim. Biophys. Acta, Molecular mass:4 119.5 kDa (electrophoresis) 912(3), 417-423 (1987). Isoelectric point (pI):5 4.7–5 4. Gillespie, J.P. et al., Comp. Biochem. Physiol. Pt. pH optimum: 6–7 C, 98(2-3), 351-358 (1991). 5. Robb, D.A., and Gutteridge, S., Phytochemistry, This product is isolated from the mushroom species 20(7), 1481-1485 (1981). Agaricus bisporus.6 The product was dialyzed against 6. Kertesz, D., and Zito, R., Biochim. Biophys. Acta, deionized water prior to lyophilization. This enzyme is 96(3), 447-462 (1965). also assayed for polyphenol oxidase and catechol 7. Kertesz, D. et al., Biochem. Biophys. Res. oxidase activities. Commun., 49(5), 1208-1215 (1972).

RBG,GCY,MAM 03/18-1 Activity: 1,000 units/mg solid

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